Can Recombinant Human VEGF R1/Flt-1 Fc Chimera (Catalog # 321-FL) block the activity of Mouse VEGF?

Name: Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein
Brand: R&D Systems
SKU: 321-FL
Rating: 5 (11 reviews)

Yes. In our testing of HUVECs, catalog # 321-FL blocks recombinant mouse VEGF as well as it blocks recombinant human VEGF.

Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein

R&D Systems, Inc. a Bio-Techne Brand

Catalog # 321-FL

Citations (41)

(11)

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Setting the standard in quality research reagents

Key Product Details

Source:	Sf 21 (baculovirus)
Accession #:	AAC50060
Structure / Form:	Disulfide-linked homodimer
Applications:	Bioactivity

View Full Technical Details for Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein

Product Specifications for Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein

Source

Spodoptera frugiperda, Sf 21 (baculovirus)-derived human VEGFR1/Flt-1 protein

Human VEGFR1 (Ser27-His687) Accession # AAC50060	IEGRMD	Human IgG₁ (Pro100-Lys330)	6-His tag
N-terminus			C-terminus

Purity

>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal sequence Analysis

Ser27

Predicted Molecular Mass

100 kDa (monomer)

SDS-PAGE

123 kDa, reducing conditions

Activity

Measured by its ability to inhibit the VEGF-dependent proliferation of HUVEC human umbilical vein endothelial cells. Conn, G. et al. (1990) Proc. Natl. Acad. Sci. USA 87:1323. The ED₅₀ for this effect is 5-30 ng/mL.

Formulation, Preparation and Storage

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

321-FL

Carrier

Formulation	Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl and CHAPS with BSA as a carrier protein.
Reconstitution	Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 3 months, 2 to 8 °C under sterile conditions after reconstitution.

321-FL/CF

Carrier Free

Formulation	Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl and CHAPS.
Reconstitution	Reconstitute at 100 μg/mL in sterile PBS.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 3 months, 2 to 8 °C under sterile conditions after reconstitution.

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: VEGFR1/Flt-1

VEGFR1 (vascular endothelial growth factor receptor 1), also called Flt-1 (Fms-like tyrosine kinase), is a 180 kDa type I transmembrane glycoprotein in the class III subfamily of receptor tyrosine kinases (RTKs) (1, 2). While family members VEGFR1, VEGFR2/KDR/Flk-1 and VEGFR3/Flt-4 are all mainly expressed on endothelial cells and play central roles in vasculogenesis, angiogenesis, and lymphangiogenesis, only VEGFR1 is expressed on macrophages, and mainly plays inhibitory roles (1-3). VEGFR1 expression is also reported on osteoblasts, placental trophoblasts, renal mesangial cells, and some hematopoietic stem cells (1, 2). Like other class III RTKs, human VEGFR1 contains a signal peptide (aa 1-22), an extracellular domain (ECD aa 27-758) with seven Ig-like repeats, a transmembrane domain (aa 759-780) and a cytoplasmic region (aa 781-1338) with a tyrosine kinase domain and several autocatalytic phosphotyrosine sites. Human VEGFR1 ECD shares 78%, 78%, 84%, 87%, and 90% aa sequence identity with mouse, rat, porcine, canine and equine VEGFR1, respectively. Soluble forms of the VEGFR1 ECD are produced by alternative splicing, and may also be shed during regulated intracellular proteolysis (4-10). Both soluble and transmembrane forms can inhibit angiogenesis by binding and sequestering its ligands, VEGF (VEGF-A), VEGF-B or PlGF (6‑11). VEGFR1 dimerizes upon ligand binding, which can include heterodimerization with VEGFR2 that modifies VEGFR2-mediated endothelial proliferation and vessel branching (8, 11, 12). VEGFR1 binds VEGF with higher affinity than does VEGFR2, but shows weaker kinase activity (9, 13). Both PlGF and VEGF induce autophosphorylation of transmembrane VEGFR1 (5, 9, 13). While deletion of mouse VEGFR1 is lethal due to overgrowth and disorganization of the vasculature, kinase-inactive mutants are viable (13, 14). VEGFR1 is up‑regulated during hypoxia, and participates in neovascularization and wound healing (1, 2, 15). VEGFR1 engagement on monocyte/macrophage lineage cells enhances their migration, and release of growth factors and cytokines (1, 3, 13, 16). Lymphangiogenesis, angiogenesis, and growth-promoting effects of VEGFR1 are thought to result from enhanced migration of macrophages from the bone marrow to tumors and tissues where they recruit endothelial progenitors (3, 16). Circulating levels of VEGFR1 increase during pregnancy and are further elevated in preeclampsia (4, 6, 17).

Item	Value
References	Otrock, Z.K. et al. (2007) Blood Cells Mol. Dis. 38:258. Peters, K.G. et al. (1993) Proc. Natl. Acad. Sci. USA 90:8915. Murakami, M. et al. (2008) Arterioscler. Thromb. Vasc. Biol. 28:658. Al-Ani, B. et al. (2010) Hypertension 55:689. Rahimi, N. et al. (2009) Cancer Res. 69:2607. He, Y. et al. (1999) Molecular Endocrinology 13:537. Cai, J. et al. (2012) EMBO Mol. Med. 4:980. Kendall, R.L. and K.A. Thomas (1993) Proc. Natl. Acad. Sci. USA 90:10705. Sawano, A. et al. (1996) Cell Growth Differ. 7:213. Barleon, B. et al. (1997) J. Biol. Chem. 272:10382. Kappas, N.C. et al. (2008) J. Cell Biol. 181:847. Mac Gabhann, F. and A.S. Popel (2007) Biophys. Chem. 128:125. Hiratsuka, S. et al. (1998) Proc. Natl. Acad. Sci. USA 95:9349. Fong, G.H. et al. (1995) Nature 376:66. Nishi, J. et al. (2008) Circ. Res. 103:261. Muramatsu, M. et al. (2010) Cancer Res. 70:8211. Levine, R.J. et al. (2004) N. Engl. J. Med. 350:672.
Long Name	Vascular Endothelial Growth Factor Receptor 1
Entrez Gene IDs	2321 (Human); 14254 (Mouse)
Alternate Names	EC 2.7.10, EC 2.7.10.1, FLT, FLT1, FRT, Flt-1, Fms-like tyrosine kinase 1, Tyrosine-protein kinase FRT, Tyrosine-protein kinase receptor FLT, VEGF R1, VEGFR-1, VEGFR1, Vascular permeability factor receptor, fms-related tyrosine kinase 1 (vascular endothelial growth factor/vascularpermeability factor receptor), vascular endothelial growth factor receptor 1

Citations for Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein (41)

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Citations are publications that use Bio-Techne products. Selected citations for Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein include:

Species: Human
Sample Types: Protein
Applications: ELISA Capture

AV Yagolovich et al. (2022), Optimized Heterologous Expression and Efficient Purification of a New TRAIL-Based Antitumor Fusion Protein SRH-DR5-B with Dual VEGFR2 and DR5 Receptor Specificity International Journal of Molecular Sciences, 23(11).
PMID: 35682540
Species: Human
Sample Types: Whole Cells
Applications: Cell Culture

A Schulz et al. (2022), The Soluble Fms-like Tyrosine Kinase-1 Contributes to Structural and Functional Changes in Endothelial Cells in Chronic Kidney Disease International Journal of Molecular Sciences, 23(24).
PMID: 36555698
Species: Human
Sample Types: Recombinant Protein
Applications: ELISA Capture

R Beckmann et al. (2021), DutaFabs are engineered therapeutic Fab fragments that can bind two targets simultaneously Nature Communications, 12(1):708.
PMID: 33514724
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

F Njau et al. (2020), Calcium dobesilate reduces VEGF signaling by interfering with heparan sulfate binding site and protects from vascular complications in diabetic mice PLoS ONE, 15(1):e0218494.
PMID: 31935212
Species: N/A
Sample Types: Protein
Applications: Surface Plasmon Resonance

SB Mamer et al. (2020), VEGF-A splice variants bind VEGFRs with differential affinities Sci Rep, 10(1):14413.
PMID: 32879419
Species: Human
Sample Types: Recombinant Protein
Applications: Bioassay

SB Mamer et al. (2020), VEGF-A splice variants bind VEGFRs with differential affinities Sci Rep, 10(1):14413.
PMID: 32879419
Species: Human
Sample Types: Recombinant Protein
Applications: Bioassay

JA Buczek-Tho et al. (2019), Hypoxia Induced Heparan Sulfate Primes the Extracellular Matrix for Endothelial Cell Recruitment by Facilitating VEGF-Fibronectin Interactions Int J Mol Sci, 20(20).
PMID: 31614727
Species: Mouse

Applications: Surface Plasmon Resonance

M Verma et al. (2019), Inhibition of FLT1 ameliorates muscular dystrophy phenotype by increased vasculature in a mouse model of Duchenne muscular dystrophy PLoS Genet., 15(12):e1008468.
PMID: 31877123
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

KC Wheeler et al. (2018), VEGF may contribute to macrophage recruitment and M2 polarization in the decidua PLoS ONE, 13(1):e0191040.
PMID: 29324807
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo

M Verma et al. (2018), Muscle Satellite Cell Cross-Talk with a Vascular Niche Maintains Quiescence via VEGF and Notch Signaling Cell Stem Cell, 23(4):530-543.e9.
PMID: 30290177
Species: Rat
Sample Types: In Vivo
Applications: In Vivo

J Gibbens et al. (2017), Dysregulation of the Fas/FasL system in an experimental animal model of HELLP syndrome Pregnancy Hypertens, 8(0):26-30.
PMID: 28501275
Species: Human
Sample Types: Recombinant Protein
Applications: Bioassay

PI Toivanen et al. (2017), Snake venom VEGF Vammin induces a highly efficient angiogenic response in skeletal muscle via VEGFR-2/NRP specific signaling Sci Rep, 7(1):5525.
PMID: 28717175
Species: Human
Sample Types: Recombinant Protein
Applications: Surface Plasmon Resonance

SB Mamer et al. (2017), Discovery of High-Affinity PDGF-VEGFR Interactions: Redefining RTK Dynamics Sci Rep, 7(1):16439.
PMID: 29180757
Sample Types: Protein
Applications: Bioassay

ME LeBlanc et al. (2017), Secretogranin III as a disease-associated ligand for antiangiogenic therapy of diabetic retinopathy J. Exp. Med, 0(0).
PMID: 28330905
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

(2016), Tumor-Derived Factors and Reduced p53 Promote Endothelial Cell Centrosome Over-Duplication PLoS ONE, 11(12):e0168334.
PMID: 27977771
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Terrance G Johns (2016), Axitinib Has Antiangiogenic and Antitumorigenic Activity in Myxoid Liposarcoma Sarcoma, 2016(0):3484673.
PMID: 27822137
Species: Human
Sample Types: Plasma
Applications: Hemofiltration Procedure

Benjamin Malard (2016), Adsorption as a Contributor for Inflammatory Mediators Removal by Different Hemofiltration Membranes: A Pilot Study Artif Organs, 0(0).
PMID: 27911005
Species: Human
Sample Types: Recombinant Protein
Applications: Enzyme Assay

Kyu-Yeon Han et al. (2016), Proangiogenic Interactions of Vascular Endothelial MMP14 With VEGF Receptor 1 in VEGFA-Mediated Corneal Angiogenesis. Investigative Ophthalmology Visual Science, 2016;0(0):1552-5783.
PMID: 27327585
Species: Human
Sample Types: Protein
Applications: Bioassay

Teran M et al. (2015), Synergistic Binding of Vascular Endothelial Growth Factor-A and Its Receptors to Heparin Selectively Modulates Complex Affinity. J Biol Chem, 290(26):16451-62.
PMID: 25979342
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Yi K et al. (2014), Effects of sFlt-1 and alpha 2-macroglobulin on vascular endothelial growth factor-induced endothelin-1 upregulation in human microvascular endothelial cells. Placenta, 35(1):64-9.
PMID: 24231447
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Orecchia A et al. (2014), Endothelial cell adhesion to soluble vascular endothelial growth factor receptor-1 triggers a cell dynamic and angiogenic phenotype. FASEB J, 28(2):692-704.
PMID: 24174428
Species: Human
Sample Types: Recombinant Protein
Applications: Competitive ELISA

Qi et al. (2013), Tissue inhibitor of metalloproteinases-3 peptides inhibit angiogenesis and choroidal neovascularization in mice. PLoS ONE, 8(3):e55667.
PMID: 23469166
Species: Rat
Sample Types: In Vivo
Applications: In Vivo

Schreurs MP et al. (2012), The adaptation of the blood-brain barrier to vascular endothelial growth factor and placental growth factor during pregnancy. FASEB J., 26(1):355-62.
PMID: 21911594
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Tabata T et al. (2012), Cytomegalovirus impairs cytotrophoblast-induced lymphangiogenesis and vascular remodeling in an in vivo human placentation model. Am J Pathol, 181(5):1540-59.
PMID: 22959908
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay

Franco M et al. (2011), Pericytes promote endothelial cell survival through induction of autocrine VEGF-A signaling and Bcl-w expression. Blood, 118(10):2906-17.
PMID: 21778339
Species: Human
Sample Types: Recombinant Protein
Applications: Binding Assay

Goyal A et al. (2011), Endorepellin, the angiostatic module of perlecan, interacts with both the alpha2beta1 integrin and vascular endothelial growth factor receptor 2 (VEGFR2): a dual receptor antagonism. J. Biol. Chem., 286(29):25947-62.
PMID: 21596751
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Lorquet S et al. (2010), Soluble forms of VEGF receptor-1 and -2 promote vascular maturation via mural cell recruitment. FASEB J., 24(10):3782-95.
PMID: 20484670
Species: Porcine
Sample Types: Aqueous Humor
Applications: Bioassay

Nishiguchi KM et al. (2010), Regulation of pathologic retinal angiogenesis in mice and inhibition of VEGF-VEGFR2 binding by soluble heparan sulfate. PLoS ONE, 5(10):e13493.
PMID: 20975989
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Kishuku M et al. (2009), Expression of soluble vascular endothelial growth factor receptor-1 in human monocyte-derived mature dendritic cells contributes to their antiangiogenic property. J. Immunol., 183(12):8176-85.
PMID: 20007583
Species: Human
Sample Types: Recombinant Protein
Applications: Bioassay

Rennel ES et al. (2009), VEGF(121)b, a new member of the VEGF(xxx)b family of VEGF-A splice isoforms, inhibits neovascularisation and tumour growth in vivo. Br. J. Cancer, 101(7):1183-93.
PMID: 19707198
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Ponticelli S et al. (2008), Modulation of angiogenesis by a tetrameric tripeptide that antagonizes vascular endothelial growth factor receptor 1. J. Biol. Chem., 283(49):34250-9.
PMID: 18922791
Species: N/A
Sample Types: N/A
Applications: ELISA (Standard)

Narazaki M et al. (2006), Ligand-induced internalization selects use of common receptor neuropilin-1 by VEGF165 and semaphorin3A. Blood, 107(10):3892-901.
PMID: 16424390
Species: Human
Sample Types: Buffer
Applications: Bioassay

Lake AC et al. (2006), Low molecular weight fucoidan increases VEGF165-induced endothelial cell migration by enhancing VEGF165 binding to VEGFR-2 and NRP1. J. Biol. Chem., 281(49):37844-52.
PMID: 17028197
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Red-Horse K et al. (2006), Cytotrophoblast induction of arterial apoptosis and lymphangiogenesis in an in vivo model of human placentation. J. Clin. Invest., 116(10):2643-52.
PMID: 16998586
Species: Primate - Macaca mulatta (Rhesus Macaque)
Sample Types: In Vivo
Applications: In Vivo

Xu F et al. (2005), Intraovarian actions of anti-angiogenic agents disrupt periovulatory events during the menstrual cycle in monkeys. Contraception, 71(4):239-48.
PMID: 15792643
Species: Porcine
Sample Types: Whole Cells
Applications: Bioassay

Seo KH et al. (2004), Estrogen enhances angiogenesis through a pathway involving platelet-activating factor-mediated nuclear factor-kappaB activation. Cancer Res., 64(18):6482-8.
PMID: 15374958
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo

Kodama I et al. (2004), Estrogen regulates the production of VEGF for osteoclast formation and activity in op/op mice. J. Bone Miner. Res., 19(2):200-6.
PMID: 14969389
Species: N/A
Sample Types: N/A
Applications: ELISA (Standard)

Caine GJ et al. (2003), Plasma angiopoietin-1, angiopoietin-2 and Tie-2 in breast and prostate cancer: a comparison with VEGF and Flt-1. Eur. J. Clin. Invest., 33(10):883-90.
PMID: 14511360
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Maynard SE et al. (2003), Excess placental soluble fms-like tyrosine kinase 1 (sFlt1) may contribute to endothelial dysfunction, hypertension, and proteinuria in preeclampsia. J. Clin. Invest., 111(5):649-58.
PMID: 12618519
Species: Avian - Quail
Sample Types: Whole Tissue
Applications: Bioassay

Argraves WS et al. (2002), VEGF signaling is required for the assembly but not the maintenance of embryonic blood vessels. Dev. Dyn., 225(3):298-304.
PMID: 12412012
Species: Human
Sample Types: Buffer
Applications: Binding Assay

Arap W et al. (2002), Steps toward mapping the human vasculature by phage display. Nat. Med., 8(2):121-7.
PMID: 11821895

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Customer Reviews for Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein (11)

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Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein

Name: Anonymous

Application: Co-immunoprecipitation study

Verified Customer | Posted 08/05/2020
Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Name: Anonymous

Application: SDS-PAGE Control

Verified Customer | Posted 04/12/2018
Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Name: Anonymous

Application: Binding assay/Protein-protein interaction

Verified Customer | Posted 03/30/2018
Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Name: Anonymous

Application: SDS-PAGE Control

Verified Customer | Posted 03/15/2018
Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Name: Lea David

Application: SDS-PAGE Control

Verified Customer | Posted 03/11/2018
Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Name: Anonymous

Application: Binding assay/Protein-protein interaction

Verified Customer | Posted 11/27/2017
Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Name: Anonymous

Application: Binding assay/Protein-protein interaction

Verified Customer | Posted 11/18/2017
Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Name: Anonymous

Application: In vitro bioactivity in cell culture

Verified Customer | Posted 11/10/2017
Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Name: Anonymous

Application: Surface plasma resonance

Verified Customer | Posted 10/23/2017
Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Name: Anonymous

Application: Immunoassay Standard

Verified Customer | Posted 07/29/2017
Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Name: Anonymous

Application: Binding assay/Protein-protein interaction

Verified Customer | Posted 07/29/2017

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FAQs for Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein

Can Recombinant Human VEGF R1/Flt-1 Fc Chimera (Catalog # 321-FL) block the activity of Mouse VEGF?

Yes. In our testing of HUVECs, catalog # 321-FL blocks recombinant mouse VEGF as well as it blocks recombinant human VEGF.

Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein

R&D Systems, Inc. a Bio-Techne Brand

Key Product Details

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Product Specifications for Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein

Formulation, Preparation and Storage

Carrier Free

321-FL

Carrier

321-FL/CF

Carrier Free

Reconstitution Calculator

Background: VEGFR1/Flt-1

Citations for Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein (41)

Customer Reviews for Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein (11)

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Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein

Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

Recombinant Human VEGF R1/Flt-1 Fc Chimera Protein

FAQs for Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein

Product Documents for Recombinant Human VEGFR1/Flt-1 Fc Chimera Protein

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